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dc.contributor.authorOgoyi, Dorington O.
dc.contributor.authorOsir, Ellie O.
dc.contributor.authorOlembo, Norah K.
dc.date.accessioned2013-06-26T06:00:56Z
dc.date.available2013-06-26T06:00:56Z
dc.date.issued1995-11
dc.identifier.citationOgoyi, Dorington O, Olembo, Norah K. P Osir, Ellie O .Comparative Biochemistry and Physiology Part B :Biochemistry and Molecular Biology Volume 112, Issue 3, November 1995, Pages 441–449en
dc.identifier.urihttp://erepository.uonbi.ac.ke:8080/xmlui/handle/123456789/40032
dc.description.abstractLipophorin was isolated from the hemolymph by KBr density gradient ultracentrifugation. Apolipophorin-III (apoLp-III) was isolated from low-density lipophorin (LDLp). High-density lipophorin (HDLp) (Mr ∼-620,000) consisted of two apoproteins, apoLp-I (Mr ∼-224,000) and apoLp-II (Mr ∼-81,000). Isolated apoLp-III (Mr ∼-20,000) had two isoforms in non-denaturing gels. Injection of adipokinetic hormone-I resulted in the formation of LDLp in both locust phases. Lipid content of HDLp was estimated at 48.4% and 51.8% for solitary and gregarious locusts, respectively. In LDLp, lipids constituted 59.8% and 57.1% for gregarious and solitary locusts, respectively. The results suggest that the gregarious locusts were more efficient in the conversion of HDLp to LDLp.en
dc.language.isoenen
dc.publisherUniversity of Nairobien
dc.titleComparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biologyen
dc.typeArticleen
local.publisherDepartment of Biochemistry, University of Nairobien


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